SitesBLAST
Comparing HSERO_RS19935 HSERO_RS19935 hydrolase to proteins with known functional sites using BLASTp with E ≤ 0.001.
Or try Sites on a Tree, PaperBLAST, Conserved Domains, or compare to all protein structures
Found 20 (the maximum) hits to proteins with known functional sites (download)
2xuaH Crystal structure of the enol-lactonase from burkholderia xenovorans lb400 (see paper)
37% identity, 60% coverage: 164:417/420 of query aligns to 11:259/261 of 2xuaH
- active site: L32 (= L187), M98 (= M253), D214 (= D371), H241 (= H399)
- binding laevulinic acid: L32 (= L187), W132 (= W289), R135 (= R292), V151 (= V308), R154 (= R311), W155 (≠ Y312), Y183 (= Y340), A216 (≠ G373)
4uheA Structural studies of a thermophilic esterase from thermogutta terrifontis (malate bound) (see paper)
30% identity, 54% coverage: 181:406/420 of query aligns to 28:256/272 of 4uheA
- active site: F34 (≠ L187), L99 (= L251), S100 (= S252), M101 (= M253), D124 (≠ N276), E164 (= E315), D221 (= D371), H249 (= H399), L250 (≠ V400)
- binding d-malate: G33 (≠ A186), F34 (≠ L187), S100 (= S252), M101 (= M253), Y104 (≠ M256), R138 (≠ W289), M196 (≠ V347), I223 (≠ G373), H249 (= H399)
4uhfA Structural studies of a thermophilic esterase from thermogutta terrifontis (l37a mutant with butyrate bound) (see paper)
31% identity, 54% coverage: 181:406/420 of query aligns to 28:256/278 of 4uhfA
- active site: F34 (≠ L187), L99 (= L251), S100 (= S252), M101 (= M253), D124 (≠ N276), E164 (= E315), D221 (= D371), H249 (= H399), L250 (≠ V400)
- binding butanoic acid: G33 (≠ A186), F34 (≠ L187), S100 (= S252), H249 (= H399), L250 (≠ V400)
4uhdA Structural studies of a thermophilic esterase from thermogutta terrifontis (acetate bound) (see paper)
30% identity, 54% coverage: 181:406/420 of query aligns to 28:256/274 of 4uhdA
- active site: F34 (≠ L187), L99 (= L251), S100 (= S252), M101 (= M253), D124 (≠ N276), E164 (= E315), D221 (= D371), H249 (= H399), L250 (≠ V400)
- binding acetate ion: G33 (≠ A186), F34 (≠ L187), L99 (= L251), S100 (= S252), M101 (= M253), Y104 (≠ M256), R138 (≠ W289), M196 (≠ V347), H249 (= H399)
- binding magnesium ion: A233 (≠ V383), I236 (= I386), S239 (≠ A389)
6eb3C Structural and enzymatic characterization of an esterase from a metagenomic library
31% identity, 58% coverage: 164:408/420 of query aligns to 11:250/262 of 6eb3C
6eb3B Structural and enzymatic characterization of an esterase from a metagenomic library
31% identity, 58% coverage: 164:408/420 of query aligns to 11:256/268 of 6eb3B
6eb3A Structural and enzymatic characterization of an esterase from a metagenomic library
32% identity, 58% coverage: 164:408/420 of query aligns to 11:253/265 of 6eb3A
5frdA Structure of a thermophilic esterase (see paper)
29% identity, 59% coverage: 175:420/420 of query aligns to 18:249/256 of 5frdA
- binding coenzyme a: G115 (≠ T278), A116 (≠ S279), R117 (≠ Q290), L118 (≠ Q291), R119 (= R292), V120 (≠ I293), L121 (≠ A294), C172 (= C344), L178 (≠ V350), K201 (≠ Q372), L202 (≠ G373), Y207 (≠ M378), F210 (≠ A381)
3heaA The l29p/l124i mutation of pseudomonas fluorescens esterase (see paper)
28% identity, 56% coverage: 181:417/420 of query aligns to 22:269/271 of 3heaA
- active site: W28 (≠ L187), S94 (= S252), M95 (= M253), L118 (≠ A271), G119 (≠ L272), D222 (= D371), H251 (= H399)
- binding ethyl acetate: G27 (≠ A186), W28 (≠ L187), F93 (≠ L251), S94 (= S252), M95 (= M253), F198 (≠ V347), I224 (≠ G373), H251 (= H399)
3hi4A Switching catalysis from hydrolysis to perhydrolysis in p. Fluorescens esterase (see paper)
28% identity, 56% coverage: 181:417/420 of query aligns to 22:269/271 of 3hi4A
3ia2A Pseudomonas fluorescens esterase complexed to the r-enantiomer of a sulfonate transition state analog (see paper)
28% identity, 56% coverage: 181:417/420 of query aligns to 22:269/271 of 3ia2A
- active site: W28 (≠ L187), S94 (= S252), M95 (= M253), G119 (≠ L272), D222 (= D371), H251 (= H399)
- binding (2R)-butane-2-sulfonate: G27 (≠ A186), W28 (≠ L187), S94 (= S252), M95 (= M253), F125 (≠ T278), F198 (≠ V347), I224 (≠ G373), H251 (= H399)
P22862 Arylesterase; Aryl-ester hydrolase; Carboxylic acid perhydrolase; PFE; Putative bromoperoxidase; EC 3.1.1.2; EC 1.-.-.- from Pseudomonas fluorescens (see 5 papers)
28% identity, 56% coverage: 181:417/420 of query aligns to 23:270/272 of P22862
- W29 (≠ L187) binding
- L30 (≠ G188) mutation to I: 125-fold increase in catalytic efficiency for perhydrolase activity with acetic acid as substrate. 2-fold decrease in catalytic efficiency for perhydrolase activity with ethyl acetate as substrate. 1.5-fold increase in catalytic efficiency for hydrolase activity with ethyl acetate as substrate. 2.4-fold increase in kcat for hydrolysis of peracetic acid.; mutation to P: Shows faster acetyl-enzyme formation. Tenfold more efficient at hydrolysis than perhydrolysis with methyl acetate as substrate. 3-fold decrease in catalytic efficiency for hydrolase activity with methyl acetate as substrate. 15-fold decrease in catalytic efficiency for perhydrolase activity with methyl acetate as substrate (PubMed:22618813). 100-fold decrease in hydrolase activity with 4-nitrophenyl acetate as substrate. 28-fold increase in perhydrolase activity with acetate as substrate (PubMed:15803517). 100-fold increase in catalytic efficiency with acetic acid as substrate. 50-fold increase in catalytic efficiency with acetic acid as substrate; when associated with H-58 (PubMed:20112920).
- F58 (≠ H215) mutation to H: 50-fold increase in catalytic efficiency with acetic acid as substrate; when associated with P-30.
- Y70 (≠ M227) mutation to M: Does not affect esterase and perhydrolase activities.
- M96 (= M253) binding ; mutation to T: 4-fold decrease in esterase activity. Loss of perhydrolase activity.
- D100 (vs. gap) mutation to E: Small decrease in esterase and perhydrolase activities.
- T123 (≠ A275) mutation to P: Does not affect esterase and perhydrolase activities.
- F228 (≠ V376) mutation to I: 3-fold increase in esterase activity. No change in perhydrolase activity.
Sites not aligning to the query:
- 1 modified: Initiator methionine, Removed
5h3hB Esterase (eaest) from exiguobacterium antarcticum (see paper)
25% identity, 56% coverage: 181:417/420 of query aligns to 24:266/269 of 5h3hB
- active site: W30 (≠ L187), S96 (= S252), M97 (= M253), G121 (≠ N276), D220 (= D371), H248 (= H399)
- binding ethaneperoxoic acid: G29 (≠ A186), W30 (≠ L187), S96 (= S252), M97 (= M253), F127 (≠ W289), F164 (= F317), L196 (≠ T349), H248 (= H399)
1m33A Crystal structure of bioh at 1.7 a (see paper)
26% identity, 56% coverage: 181:416/420 of query aligns to 14:250/256 of 1m33A
5cbkA Crystal structure of the strigolactone receptor shhtl5 from striga hermonthica (see paper)
24% identity, 55% coverage: 180:408/420 of query aligns to 19:255/271 of 5cbkA
Sites not aligning to the query:
Q988D4 2-(acetamidomethylene)succinate hydrolase; alpha-(N-acetylaminomethylene)succinic acid amidohydrolase; AAMS amidohydrolase; EC 3.5.1.29 from Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099) (Mesorhizobium loti (strain MAFF 303099)) (see paper)
31% identity, 35% coverage: 167:312/420 of query aligns to 25:168/278 of Q988D4
- I41 (≠ L187) binding
- S106 (= S252) mutation to A: Loss of catalytic activity.
- D130 (≠ N276) mutation to N: Loss of catalytic activity.
Sites not aligning to the query:
- 230 S→A: Loss of catalytic activity.
5z7yA Crystal structure of striga hermonthica htl7 (shhtl7) (see paper)
24% identity, 54% coverage: 180:406/420 of query aligns to 18:252/267 of 5z7yA
7c8lA Hybrid designing of potent inhibitors of striga strigolactone receptor shhtl7 (see paper)
24% identity, 54% coverage: 180:406/420 of query aligns to 17:251/268 of 7c8lA
- binding 2-(2-{2-[2-(2-{2-[2-(2-{2-[4-(1,1,3,3-tetramethyl-butyl)-phenoxy]-ethoxy}-ethoxy)-ethoxy]-ethoxy}-ethoxy)-ethoxy]-ethoxy}-ethoxy)-ethanol: F132 (≠ W289), V136 (≠ I304), M137 (≠ A305), T140 (≠ V308), L151 (vs. gap), T155 (vs. gap), T188 (vs. gap), M217 (≠ G373)
- binding pyrrolidine-1-carbaldehyde: S93 (= S252), M94 (= M253), M97 (= M256), T119 (= T278), I191 (≠ V347), L194 (≠ V350), H244 (= H399)
Q9AQM4 2-hydroxy-6-oxo-6-(2'-aminophenyl)hexa-2,4-dienoic acid hydrolase; HOPDA; EC 3.7.1.13 from Pseudomonas resinovorans (see paper)
26% identity, 53% coverage: 194:417/420 of query aligns to 55:279/290 of Q9AQM4